6RSL

Cytochrome c co-crystallized with 10 eq. sulfonato-calix[8]arene and 25 eq. spermine (dry-coating method) - structure III

Summary for 6RSL

• Entry DOI: 10.2210/pdb6rsl/pdb
• Related: 6GD9 6GDA
• Descriptor: Cytochrome c iso-1, HEME C, sulfonato-calix[8]arene, ... (6 entities in total)
• Functional Keywords: molecular glues, molecular switch, spermine, polyamine, calixarene, supramolecular chemistry, oxidoreductase, cytc
• Biological source: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
• Total number of polymer chains: 2
• Total formula weight: 36260.40

Authors

Engilberge, S.,Crowley, P.B. (deposition date: 2019-05-21, release date: 2019-09-18, Last modification date: 2024-11-13)

Primary citation

Engilberge, S.,Rennie, M.L.,Dumont, E.,Crowley, P.B.
Tuning Protein Frameworks via Auxiliary Supramolecular Interactions.
Acs Nano, 13:10343-10350, 2019

PubMed Abstract: Protein crystals with their precise, periodic array of functional building blocks have potential applications in biomaterials, sensing, and catalysis. This paper describes how a highly porous crystalline framework of a cationic redox protein and an anionic macrocycle can be modulated by a small cationic effector. Ternary composites of protein (∼13 kDa), calix[8]arene (∼1.5 kDa), and effector (∼0.2 kDa) formed distinct crystalline architectures, dependent on the effector concentration and the crystallization technique. A combination of X-ray crystallography and density functional theory (DFT) calculations was used to decipher the framework variations, which appear to be dependent on a calixarene conformation change mediated by the effector. This "switch" calixarene was observed in three states, each of which is associated with a different interaction network. Two structures obtained by co-crystallization with the effector contained an additional protein "pillar", resulting in framework duplication and decreased porosity. These results suggest how protein assembly can be engineered by supramolecular host-guest interactions.

PubMed: 31490058
DOI: 10.1021/acsnano.9b04115

Experimental method

X-RAY DIFFRACTION (1.988 Å)